|
Name |
Accession |
Description |
Interval |
E-value |
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
53-487 |
0e+00 |
|
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, carboxypeptidase S, carboxypeptidase a, carboxypeptidase yscS, glycine carboxypeptidase)-like subfamily. This group mostly contains proteins that have been uncharacterized to date, but also includes vacuolar proteins involved in nitrogen metabolism which are essential for use of certain peptides that are sole nitrogen sources. YscS releases a C-terminal amino acid from a peptide that has glycine as the penultimate residue. It is synthesized as one polypeptide chain precursor which yields two active precursor molecules after carbohydrate modification in the secretory pathway. The proteolytically unprocessed forms are associated with the membrane, whereas the mature forms of the enzyme are soluble. Enzymes in this subfamily may also cleave intracellularly generated peptides in order to recycle amino acids for protein synthesis. Also included in this subfamily is peptidase M20 domain containing 1 (PM20D1), that is enriched in uncoupling protein 1, UCP1(+) versus UCP1(-) adipocytes is a bidirectional enzyme in vitro, catalyzing both the condensation of fatty acids and amino acids to generate N-acyl amino acids and also the reverse hydrolytic reaction; N-acyl amino acids directly bind mitochondria and function as endogenous uncouplers of UCP1-independent respiration. Mice studies show increased circulating PM20D1 augments respiration and increases N-acyl amino acids in blood, and administration of N-acyl amino acids improves glucose homeostasis and increases energy expenditure.
Pssm-ID: 349923 [Multi-domain] Cd Length: 471 Bit Score: 543.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 53 EALKGAIQIPTVTFS-----SEKSNTTALAEFGKYIHKVFPTVvsTSFIQHEVVEEYSHLFTIQGSDPSLQPYLLMAHFD 127
Cdd:cd05674 2 ERLSGAVQIPTVSFDdmppiDEDERWDAFYKFHDYLEKTFPLV--HKTLKVEVVNEYGLLYTWEGSDPSLKPLLLMAHQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 128 VVPAPEE---GWEVPPFSGLERDGIIYGRGTLDDKNSVMALLQALELLLIRKYIPRRSFFISLGHDEESSGT-GAQRISA 203
Cdd:cd05674 80 VVPVNPEtedQWTHPPFSGHYDGGYIWGRGALDDKNSLIGILEAVELLLKRGFKPRRTIILAFGHDEEVGGErGAGAIAE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 204 -LLQSRGVQ-LAFIVDEGGFILDDFIpnFKKPIALIAVSEKGSMNLMLQVNMTSGHSSAPPKETSIGILAAAVSRLEQTP 281
Cdd:cd05674 160 lLLERYGVDgLAAILDEGGAVLEGVF--LGVPFALPGVAEKGYMDVEITVHTPGGHSSVPPKHTGIGILSEAVAALEANP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 282 MPIIFGSG-TVVTVLQQLANEFPFPVNIILSNPWLFEPLI-----SRFMERNPLTNAIIRTTTALTIFKAGVKFNVIPPV 355
Cdd:cd05674 238 FPPKLTPGnPYYGMLQCLAEHSPLPPRSLKSNLWLASPLLkallaSELLSTSPLTRALLRTTQAVDIINGGVKINALPET 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 356 AQATVNFRIHPGQTVQEVLELTKNIVADNRVQFHV-------------------LSAFDPLPVSPSDDKALGYQLLRQTV 416
Cdd:cd05674 318 ATATVNHRIAPGSSVEEVLEHVKNLIADIAVKYGLglsafggdviystngtkllTSLLSPEPSPVSSTSSPVWQLLAGTI 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 269846968 417 QSVF---PEVNITAPVTSIGNTDSRFFTNLTTGIYRFYPIYIQPEDFKRIHGVNEKISVQAYETQVKFIFELIQ 487
Cdd:cd05674 398 RQVFeqfGEDLVVAPGIMTGNTDTRHYWNLTKNIYRFTPIRLNPEDLGRIHGVNERISIDDYLETVAFYYQLIQ 471
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
35-490 |
3.73e-168 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 483.68 E-value: 3.73e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 35 RASRIPSQF---SKEERVAMKEA-----LKGAIQIPTVT-FSSEKSNTTALAEFGKYIHKVFPTVVSTsfIQHEVVEEYS 105
Cdd:PRK08262 22 RTFRFKSRQidvPAVAPVAVDEDaaaerLSEAIRFRTISnRDRAEDDAAAFDALHAHLEESYPAVHAA--LEREVVGGHS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 106 HLFTIQGSDPSLQPYLLMAHFDVVPAP---EEGWEVPPFSGLERDGIIYGRGTLDDKNSVMALLQALELLLIRKYIPRRS 182
Cdd:PRK08262 100 LLYTWKGSDPSLKPIVLMAHQDVVPVApgtEGDWTHPPFSGVIADGYVWGRGALDDKGSLVAILEAAEALLAQGFQPRRT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 183 FFISLGHDEESSGTGAQRISALLQSRGVQLAFIVDEGGFILDDFIPNFKKPIALIAVSEKGSMNLMLQVNMTSGHSSAPP 262
Cdd:PRK08262 180 IYLAFGHDEEVGGLGARAIAELLKERGVRLAFVLDEGGAITEGVLPGVKKPVALIGVAEKGYATLELTARATGGHSSMPP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 263 KETSIGILAAAVSRLEQTPMPIIFgSGTVVTVLQQLANEFPFPVNIILSNPWLFEPLISRFMERNPLTNAIIRTTTALTI 342
Cdd:PRK08262 260 RQTAIGRLARALTRLEDNPLPMRL-RGPVAEMFDTLAPEMSFAQRVVLANLWLFEPLLLRVLAKSPETAAMLRTTTAPTM 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 343 FKAGVKFNVIPPVAQATVNFRIHPGQTVQEVLELTKNIVADNRVQFHVLSA-FDPLPVSPSDDKalGYQLLRQTVQSVFP 421
Cdd:PRK08262 339 LKGSPKDNVLPQRATATVNFRILPGDSVESVLAHVRRAVADDRVEIEVLGGnSEPSPVSSTDSA--AYKLLAATIREVFP 416
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 269846968 422 EVnITAPVTSIGNTDSRFFTNLTTGIYRFYPIYIQPEDFKRIHGVNEKISVQAYETQVKFIFELIQNAD 490
Cdd:PRK08262 417 DV-VVAPYLVVGATDSRHYSGISDNVYRFSPLRLSPEDLARFHGTNERISVANYARMIRFYYRLIENAA 484
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
59-487 |
9.69e-72 |
|
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, carboxypeptidase S, carboxypeptidase a, carboxypeptidase yscS, glycine carboxypeptidase)-like subfamily. This group contains proteins that have been uncharacterized to date with similarity to vacuolar proteins involved in nitrogen metabolism which are essential for use of certain peptides that are sole nitrogen sources. YscS releases a C-terminal amino acid from a peptide that has glycine as the penultimate residue. It is synthesized as one polypeptide chain precursor which yields two active precursor molecules after carbohydrate modification in the secretory pathway. The proteolytically unprocessed forms are associated with the membrane, whereas the mature forms of the enzyme are soluble. Enzymes in this subfamily may also cleave intracellularly generated peptides in order to recycle amino acids for protein synthesis.
Pssm-ID: 349924 [Multi-domain] Cd Length: 431 Bit Score: 234.18 E-value: 9.69e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 59 IQIPTVTFSSEKSNTTALAEF-GKYIHKV-FPTVvstSFIQHEVVEEYSHLFTIQGSDPSLQPYLLMAHFDVVPAPEEGW 136
Cdd:cd05675 8 IRIDTTNSGDGTGSETRAAEVlAARLAEAgIQTE---IFVVESHPGRANLVARIGGTDPSAGPLLLLGHIDVVPADASDW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 137 EVPPFSGLERDGIIYGRGTLDDKNSVMALLQALELLLIRKYIPRRSFFISLGHDEESSGT-GAQRISALLQSRGVQLAFI 215
Cdd:cd05675 85 SVDPFSGEIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREGFKPKRDLVFAFVADEEAGGEnGAKWLVDNHPELFDGATFA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 216 VDEGGFILddfIPNFKKPIAL-IAVSEKGSMNLMLQVNMTSGHSSAPPKETSIGILAAAVSRLEQTPMPIIFGSGTVVTV 294
Cdd:cd05675 165 LNEGGGGS---LPVGKGRRLYpIQVAEKGIAWMKLTVRGRAGHGSRPTDDNAITRLAEALRRLGAHNFPVRLTDETAYFA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 295 lqQLANEFPFPVNIILSNP-WLFEPLISRFMERNPLTNAIIRTTTALTIFKAGVKFNVIPPVAQATVNFRIHPGQTVQEV 373
Cdd:cd05675 242 --QMAELAGGEGGALMLTAvPVLDPALAKLGPSAPLLNAMLRNTASPTMLDAGYATNVLPGRATAEVDCRILPGQSEEEV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 374 LELTKNIVADNRVQFHVLSAfDPLPVSPSDDKAlgYQLLRQTVQSVFPEVNITaPVTSIGNTDSRFFTNLTTGIYRFYPI 453
Cdd:cd05675 320 LDTLDKLLGDPDVSVEAVHL-EPATESPLDSPL--VDAMEAAVQAVDPGAPVV-PYMSPGGTDAKYFRRLGIPGYGFAPL 395
|
410 420 430
....*....|....*....|....*....|....*.
gi 269846968 454 YIQPE--DFKRIHGVNEKISVQAYETQVKFIFELIQ 487
Cdd:cd05675 396 FLPPEldYTGLFHGVDERVPVESLYFGVRFLDRLVK 431
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
47-487 |
3.03e-55 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 191.75 E-value: 3.03e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 47 ERVAMKEALKGAIQIPTVtfSSEKSNTTALAEFGKYIHKV-FPtvVSTSFIQHEVVEEYSHLFTIQGSDPSlQPYLLMAH 125
Cdd:PRK09133 35 DQQAARDLYKELIEINTT--ASTGSTTPAAEAMAARLKAAgFA--DADIEVTGPYPRKGNLVARLRGTDPK-KPILLLAH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 126 FDVVPAPEEGWEVPPFSGLERDGIIYGRGTLDDKnsVMALLQALELLLIRK--YIPRRSFFISLGHDEEssGTGAQRISA 203
Cdd:PRK09133 110 MDVVEAKREDWTRDPFKLVEENGYFYGRGTSDDK--ADAAIWVATLIRLKRegFKPKRDIILALTGDEE--GTPMNGVAW 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 204 LLQSRG--VQLAFIVDEGGF-ILDDfipnFKKPIAL-IAVSEKGSMNLMLQVNMTSGHSSAPPKETSIGILAAAVSRLEQ 279
Cdd:PRK09133 186 LAENHRdlIDAEFALNEGGGgTLDE----DGKPVLLtVQAGEKTYADFRLEVTNPGGHSSRPTKDNAIYRLAAALSRLAA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 280 TPMPIIFGSGTvVTVLQQLANEFPFPV----NIILSNPwlFEPLISRFMERNPLTNAIIRTTTALTIFKAGVKFNVIPPV 355
Cdd:PRK09133 262 YRFPVMLNDVT-RAYFKQSAAIETGPLaaamRAFAANP--ADEAAIALLSADPSYNAMLRTTCVATMLEGGHAENALPQR 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 356 AQATVNFRIHPGQTVQEVLELTKNIVADNRVQFHVLSAFDPLPVSPSDDKALGyqLLRQTVQSVFPEVNITaPVTSIGNT 435
Cdd:PRK09133 339 ATANVNCRIFPGDTIEAVRATLKQVVADPAIKITRIGDPSPSPASPLRPDIMK--AVEKLTAAMWPGVPVI-PSMSTGAT 415
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 269846968 436 DSRFFTNLTTGIYRFYPIYIQPEDFkRIHGVNEKISVQAYETQVKFIFELIQ 487
Cdd:PRK09133 416 DGRYLRAAGIPTYGVSGLFGDPDDT-FAHGLNERIPVASFYEGRDFLYELVK 466
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
50-488 |
5.71e-49 |
|
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino acid transport and metabolism]; Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440389 [Multi-domain] Cd Length: 388 Bit Score: 172.76 E-value: 5.71e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 50 AMKEALKGAIQIPTVTfsseKSNTTALAEFGKYIHKV-FPTVVstsfiqHEVVEEYSHLF-TIQGSDPSlQPYLLMAHFD 127
Cdd:COG0624 13 EALELLRELVRIPSVS----GEEAAAAELLAELLEALgFEVER------LEVPPGRPNLVaRRPGDGGG-PTLLLYGHLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 128 VVPA-PEEGWEVPPFSGLERDGIIYGRGTLDDKNSVMALLQALELLLIRKYIPRRSFFISLGHDEESSGTGAQRISALLQ 206
Cdd:COG0624 82 VVPPgDLELWTSDPFEPTIEDGRLYGRGAADMKGGLAAMLAALRALLAAGLRLPGNVTLLFTGDEEVGSPGARALVEELA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 207 SRGVQLAFIVDEGGFILDdfipnfkkpialIAVSEKGSMNLMLQVNMTSGHSSAPPKETS-IGILAAAVSRLEQTPMPii 285
Cdd:COG0624 162 EGLKADAAIVGEPTGVPT------------IVTGHKGSLRFELTVRGKAAHSSRPELGVNaIEALARALAALRDLEFD-- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 286 fgsgtvvtvlqqlanefpfpvniilsnpwlfeplisrfMERNPLTNaiiRTTTALTIFKAGVKFNVIPPVAQATVNFRIH 365
Cdd:COG0624 228 --------------------------------------GRADPLFG---RTTLNVTGIEGGTAVNVIPDEAEAKVDIRLL 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 366 PGQTVQEVLELTKNIVADN----RVQFHVLSAFDPLPVSPSDDKAlgYQLLRQTVQSVFPEVniTAPVTSIGNTDSRFFT 441
Cdd:COG0624 267 PGEDPEEVLAALRALLAAAapgvEVEVEVLGDGRPPFETPPDSPL--VAAARAAIREVTGKE--PVLSGVGGGTDARFFA 342
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 269846968 442 NlTTGIyrfyPIY-IQPEDFKRIHGVNEKISVQAYETQVKFIFELIQN 488
Cdd:COG0624 343 E-ALGI----PTVvFGPGDGAGAHAPDEYVELDDLEKGARVLARLLER 385
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
121-488 |
6.58e-36 |
|
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases.
Pssm-ID: 460247 [Multi-domain] Cd Length: 315 Bit Score: 135.55 E-value: 6.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 121 LLMAHFDVVPaPEEGWEVPpFSgLERDGIIYGRGTLDDKNSVMALLQALELLLiRKYIPRRSFFISLGHDEESSGTGAQR 200
Cdd:pfam01546 1 LLRGHMDVVP-DEETWGWP-FK-STEDGKLYGRGHDDMKGGLLAALEALRALK-EEGLKKGTVKLLFQPDEEGGMGGARA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 201 ISALLQSRGVQLAFIVdeGGFILDDFIPNFKKPIAlIAVSEKGSMNLMLQVNMTSGHSSAPPK-ETSIGILAAAVSRLEQ 279
Cdd:pfam01546 77 LIEDGLLEREKVDAVF--GLHIGEPTLLEGGIAIG-VVTGHRGSLRFRVTVKGKGGHASTPHLgVNAIVAAARLILALQD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 280 tpmpiifgsgtvvtvlqqlanefpfpvniilsnpwlfepLISRfmERNPLTNAIIrTTTALTIFKAGvkFNVIPPVAQAT 359
Cdd:pfam01546 154 ---------------------------------------IVSR--NVDPLDPAVV-TVGNITGIPGG--VNVIPGEAELK 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 360 VNFRIHPGQTVQEVLELTKNIVADNRVQFHVLSAFDPLPVSP---SDDKALgYQLLRQTVQSVFPEVNITAPVTSIGNTD 436
Cdd:pfam01546 190 GDIRLLPGEDLEELEERIREILEAIAAAYGVKVEVEYVEGGApplVNDSPL-VAALREAAKELFGLKVELIVSGSMGGTD 268
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 269846968 437 SRFFTNlttGIYRFYPIYIQPEDfkRIHGVNEKISVQAYETQVKFIFELIQN 488
Cdd:pfam01546 269 AAFFLL---GVPPTVVFFGPGSG--LAHSPNEYVDLDDLEKGAKVLARLLLK 315
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
110-474 |
2.13e-35 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 136.91 E-value: 2.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 110 IQGSDPSLQPYLLMAHFDVVPAPEEGWEVPPFSGLERDGIIYGRGTLDDKNSVMALLQALELLLIRKYIPRRSFFISLGH 189
Cdd:PRK07906 58 LPGADPSRPALLVHGHLDVVPAEAADWSVHPFSGEIRDGYVWGRGAVDMKDMDAMMLAVVRHLARTGRRPPRDLVFAFVA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 190 DEESSGT-GAQrisALLQSR-----GVQLAfIVDEGGFILDDfipNFKKPIALIAVSEKGSMNLMLQVNMTSGHSSAPPK 263
Cdd:PRK07906 138 DEEAGGTyGAH---WLVDNHpelfeGVTEA-ISEVGGFSLTV---PGRDRLYLIETAEKGLAWMRLTARGRAGHGSMVND 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 264 ETSIGILAAAVSRLEQTPMPIIFgSGTVVTVLQQLANEF--PFPvniiLSNPwlfEPLISRFMERNPLTNAIIRTTTALT 341
Cdd:PRK07906 211 DNAVTRLAEAVARIGRHRWPLVL-TPTVRAFLDGVAELTglEFD----PDDP---DALLAKLGPAARMVGATLRNTANPT 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 342 IFKAGVKFNVIPPVAQATVNFRIHPGQtvQEVLELTKNIVADNRVQFHVLSAFDPL--PVspsdDKALgYQLLRQTVQSV 419
Cdd:PRK07906 283 MLKAGYKVNVIPGTAEAVVDGRFLPGR--EEEFLATVDELLGPDVEREWVHRDPALetPF----DGPL-VDAMNAALLAE 355
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 269846968 420 FPEVNiTAPVTSIGNTDSRFFTNLttGI--YRFYPIYIQPE-DFKRI-HGVNEKISVQA 474
Cdd:PRK07906 356 DPGAR-VVPYMLSGGTDAKAFSRL--GIrcYGFAPLRLPPDlDFAALfHGVDERVPVDA 411
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
55-486 |
4.88e-30 |
|
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE)-like; Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) like family of enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this family are mostly bacterial and have been inferred by homology as being related to both ArgE and DapE. This family also includes N-acetyl-L-citrulline deacetylase (ACDase; acetylcitrulline deacetylase), a unique, novel enzyme found in Xanthomonas campestris, a plant pathogen, in which N-acetyl-L-ornithine is the substrate for transcarbamoylation reaction, and the product is N-acetyl-L-citrulline. Thus, in the arginine biosynthesis pathway, ACDase subsequently catalyzes the hydrolysis of N-acetyl-L-citrulline to acetate and L-citrulline.
Pssm-ID: 349944 [Multi-domain] Cd Length: 361 Bit Score: 120.48 E-value: 4.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 55 LKGAIQIPTVTfSSEKSNTTALAE-FGKYIHKVFPTVVStsfiqhevvEEYSHLFTIQGSDPSlqPYLLMAHFDVVPA-P 132
Cdd:cd08659 3 LQDLVQIPSVN-PPEAEVAEYLAElLAKRGYGIESTIVE---------GRGNLVATVGGGDGP--VLLLNGHIDTVPPgD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 133 EEGWEVPPFSGLERDGIIYGRGTLDDKNSVMALLQALELLLIRKYIPRRSFFISLGHDEESSGTGAQRISALLQSRGVqL 212
Cdd:cd08659 71 GDKWSFPPFSGRIRDGRLYGRGACDMKGGLAAMVAALIELKEAGALLGGRVALLATVDEEVGSDGARALLEAGYADRL-D 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 213 AFIVDEggfilddfipnfkkPIAL-IAVSEKGSMNLMLQVNMTSGHSSAPPKETS-IGILAAAVSRLEQtpmpiifgsgt 290
Cdd:cd08659 150 ALIVGE--------------PTGLdVVYAHKGSLWLRVTVHGKAAHSSMPELGVNaIYALADFLAELRT----------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 291 vvtvlqqlanefpfpvniilsnpwLFEPLisrfmERNPLTNAiirTTTALTIFKAGVKFNVIPPVAQATVNFRIHPGQTV 370
Cdd:cd08659 205 ------------------------LFEEL-----PAHPLLGP---PTLNVGVINGGTQVNSIPDEATLRVDIRLVPGETN 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 371 QEVLELTKNIVADNRVQFHV---LSAFDPLPVSPSDDkalgyqlLRQTVQSVFPEVNITAPV-TSIGNTDSRFFTNLTTg 446
Cdd:cd08659 253 EGVIARLEAILEEHEAKLTVevsLDGDPPFFTDPDHP-------LVQALQAAARALGGDPVVrPFTGTTDASYFAKDLG- 324
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 269846968 447 iyrfYPIYI-QPEDFKRIHGVNEKISVQAYETQVKFIFELI 486
Cdd:cd08659 325 ----FPVVVyGPGDLALAHQPDEYVSLEDLLRAAEIYKEII 361
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
53-480 |
1.41e-25 |
|
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences contains annotations for both acetylornithine deacetylase and succinyl-diaminopimelate desuccinylase, but does not contain any members with experimental characterization. Bacillus, Staphylococcus and Sulfolobus species contain multiple hits to this subfamily and each may have a separate activity. Determining which is which must await further laboratory research. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 273870 [Multi-domain] Cd Length: 375 Bit Score: 107.87 E-value: 1.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 53 EALKGAIQIPTVTFSSEKSNTTA------LAEFGKYIHKVFPTVVSTSFIQHEVVEEYSHlftiqGSDPSLqpyLLMAHF 126
Cdd:TIGR01910 2 ELLKDLISIPSVNPPGGNEETIAnyikdlLREFGFSTDVIEITDDRLKVLGKVVVKEPGN-----GNEKSL---IFNGHY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 127 DVVPA-PEEGWEVPPFSGLERDGIIYGRGTLDDKNSVMALLQALELLLIRKYIPRRSFFISLGHDEESSGTGAQrisALL 205
Cdd:TIGR01910 74 DVVPAgDLELWKTDPFKPVEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEESGEAGTL---YLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 206 QSRGVQLA---FIVDEGGFIlddfipnfkkpiaLIAVSEKGSMNLMLQVNMTSGHSSApPKETSIGILAAAvsrleqtpm 282
Cdd:TIGR01910 151 QRGYFKDAdgvLIPEPSGGD-------------NIVIGHKGSIWFKLRVKGKQAHASF-PQFGVNAIMKLA--------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 283 piifgsgtvvtvlqQLANEfpfpvniilsnpwlFEPLISRFMERNPLTNAIIRTTTALTIFKAGVKFNVIPPVAQATVNF 362
Cdd:TIGR01910 208 --------------KLITE--------------LNELEEHIYARNSYGFIPGPITFNPGVIKGGDWVNSVPDYCEFSIDV 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 363 RIHPGQTVQEVLELTKNIVADNRVQFHVLSAFDPL-----PVSPSDDKALgYQLLRQTVQSVfpeVNITAPVTSI-GNTD 436
Cdd:TIGR01910 260 RIIPEENLDEVKQIIEDVVKALSKSDGWLYENEPVvkwsgPNETPPDSRL-VKALEAIIKKV---RGIEPEVLVStGGTD 335
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 269846968 437 SRFFtnlttgIYRFYPIYI-QPEDFKRIHGVNEKISVQAYETQVK 480
Cdd:TIGR01910 336 ARFL------RKAGIPSIVyGPGDLETAHQVNEYISIKNLVESTK 374
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
54-486 |
8.05e-21 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly archaeal, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349933 [Multi-domain] Cd Length: 355 Bit Score: 93.61 E-value: 8.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 54 ALKGAIQIPTVtfSSEKSNTTALAEFGKYIHKVFPTVVSTsfiqHEVVEE-YSHLFTIQGSDPSlqPYLLM-AHFDVVPA 131
Cdd:cd08011 3 LLQELVQIPSP--NPPGDNTSAIAAYIKLLLEDLGYPVEL----HEPPEEiYGVVSNIVGGRKG--KRLLFnGHYDVVPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 132 PE-EGWEVPPFSGLERDGIIYGRGTLDDKNSVMALLQALELLLIRKYIPRRSFFISLGHDEESSGTGAQRisallqsrgv 210
Cdd:cd08011 75 GDgEGWTVDPYSGKIKDGKLYGRGSSDMKGGIAASIIAVARLADAKAPWDLPVVLTFVPDEETGGRAGTK---------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 211 qlaFIVDEGGFILDDFIpnFKKPIAL--IAVSEKGSMNLMLQVNMTSGHSSAPPketsIGILAAAVSRLeqtpmpiifgs 288
Cdd:cd08011 145 ---YLLEKVRIKPNDVL--IGEPSGSdnIRIGEKGLVWVIIEITGKPAHGSLPH----RGESAVKAAMK----------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 289 gtvvtVLQQLANEFPfpvniilsnpwlfeplisrfmernpltnaiirtTTALTIFKAGVKFNVIPPVAQATVNFRIHPGQ 368
Cdd:cd08011 205 -----LIERLYELEK---------------------------------TVNPGVIKGGVKVNLVPDYCEFSVDIRLPPGI 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 369 TVQEVLELTKNIVAD-NRVQFHVLSAFDPlpvSPSDDKALGYQLLRQTVQSVfpeVNITA-PVTSIGNTDSRFFTNltTG 446
Cdd:cd08011 247 STDEVLSRIIDHLDSiEEVSFEIKSFYSP---TVSNPDSEIVKKTEEAITEV---LGIRPkEVISVGASDARFYRN--AG 318
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 269846968 447 IyrfyP-IYIQPEDFKRIHGVNEKISVQAYETQVKFIFELI 486
Cdd:cd08011 319 I----PaIVYGPGRLGQMHAPNEYVEIDELIKVIKVHALVA 355
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
107-453 |
1.40e-19 |
|
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic N-acyl-L-amino-acid amidohydrolases active on fatty acid and acetyl amides of L-amino acids.
Pssm-ID: 273850 [Multi-domain] Cd Length: 400 Bit Score: 90.62 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 107 LFTIQGSDPSLQPYLLMAHFDVVPAPEEGWEVPPFSG-LERDGIIYGRGTLDDKNSVMALLQALELLLIRKYIPRRSFFI 185
Cdd:TIGR01880 61 VLTWPGSNPELPSILLNSHTDVVPVFREHWTHPPFSAfKDEDGNIYARGAQDMKCVGVQYLEAVRNLKASGFKFKRTIHI 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 186 SLGHDEESSG-TGAQRISALLQSRGVQLAFIVDEGGFILDDFIPNFkkpialiaVSEKGSMNLMLQVNMTSGHSSAPPKE 264
Cdd:TIGR01880 141 SFVPDEEIGGhDGMEKFAKTDEFKALNLGFALDEGLASPDDVYRVF--------YAERVPWWVVVTAPGNPGHGSKLMEN 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 265 TsigilaaAVSRLEQtpmpiifgsgTVVTVLQQLANEFPFpvniILSNPWLFEPLIsrfmernpltnaiirTTTALTIFK 344
Cdd:TIGR01880 213 T-------AMEKLEK----------SVESIRRFRESQFQL----LQSNPDLAIGDV---------------TSVNLTKLK 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 345 AGVKFNVIPPVAQATVNFRIHPGQTVQEVLELTKNIVAD--NRVQFHVLSAFDPLPVSPSDDKALGYQLLRQTVQsvfpE 422
Cdd:TIGR01880 257 GGVQSNVIPSEAEAGFDIRLAPSVDFEEMENRLDEWCADagEGVTYEFSQHSGKPLVTPHDDSNPWWVAFKDAVK----E 332
|
330 340 350
....*....|....*....|....*....|..
gi 269846968 423 VNITA-PVTSIGNTDSRFFTNLTTGIYRFYPI 453
Cdd:TIGR01880 333 MGCTFkPEILPGSTDSRYIRAAGVPALGFSPM 364
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
44-487 |
6.83e-19 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 88.51 E-value: 6.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 44 SKEERVAMKEALKGAIQIPTVTFSSEKsnttaLAEFGKYIHKVF------PTVVStsFIQHEVVEEYSHLFTIQGSDPSL 117
Cdd:PRK08651 1 VEAMMFDIVEFLKDLIKIPTVNPPGEN-----YEEIAEFLRDTLeelgfsTEIIE--VPNEYVKKHDGPRPNLIARRGSG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 118 QPYL-LMAHFDVVPaPEEGWEV-PPFSGLERDGIIYGRGTLDDKNSVMALLQALELLlirKYIPRRSFFISLGHDEESSG 195
Cdd:PRK08651 74 NPHLhFNGHYDVVP-PGEGWSVnVPFEPKVKDGKVYGRGASDMKGGIAALLAAFERL---DPAGDGNIELAIVPDEETGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 196 TGAqrisallqsrgvqlAFIVDEGGFILDDFIpnFKKPIAL--IAVSEKGSMNLMLQVNMTSGHSSAPpketSIGILAaa 273
Cdd:PRK08651 150 TGT--------------GYLVEEGKVTPDYVI--VGEPSGLdnICIGHRGLVWGVVKVYGKQAHASTP----WLGINA-- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 274 vsrleqtpmpiIFGSGTVVTVLQQLANEFPFPVNIILsnpwlfeplisrfmernPLTNAIIRTTTALTIfKAGVKFNVIP 353
Cdd:PRK08651 208 -----------FEAAAKIAERLKSSLSTIKSKYEYDD-----------------ERGAKPTVTLGGPTV-EGGTKTNIVP 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 354 PVAQATVNFRIHPGQTVQEVLELTKNIVADNRVQFHVLSAFDPLPVSP----SDDKALgYQLLRQTVQSVFpevNITAPV 429
Cdd:PRK08651 259 GYCAFSIDRRLIPEETAEEVRDELEALLDEVAPELGIEVEFEITPFSEafvtDPDSEL-VKALREAIREVL---GVEPKK 334
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 269846968 430 T-SIGNTDSRFFTNLTTGIYRFYPIyiqpeDFKRIHGVNEKISVQAYETQVKFIFELIQ 487
Cdd:PRK08651 335 TiSLGGTDARFFGAKGIPTVVYGPG-----ELELAHAPDEYVEVKDVEKAAKVYEEVLK 388
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
107-473 |
9.42e-18 |
|
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; Peptidase M20 family, proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE; aspartyl dipeptidase; succinyl-diaminopimelate desuccinylase) subfamily. DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. It has been shown that DapE is essential for cell growth and proliferation. DapEs have been purified from Escherichia coli and Haemophilus influenzae, while the genes that encode for DapEs have been sequenced from several bacterial sources such as Corynebacterium glutamicum, Helicobacter pylori, Neisseria meningitidis and Mycobacterium tuberculosis. DapE is a small, dimeric enzyme that requires two zinc atoms per molecule for full enzymatic activity. All of the amino acids that function as metal binding ligands are strictly conserved in DapE.
Pssm-ID: 349886 [Multi-domain] Cd Length: 366 Bit Score: 84.86 E-value: 9.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 107 LFTIQGSDPslqPYLLMA-HFDVVPA-PEEGWEVPPFSGLERDGIIYGRGTLDDKNSV--MALLQALELLLIRKYIPRRS 182
Cdd:cd03891 46 LWARRGTGG---PHLCFAgHTDVVPPgDLEGWSSDPFSPTIKDGMLYGRGAADMKGGIaaFVAAAERFVAKHPNHKGSIS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 183 FFISlgHDEESSGT-GAQRISALLQSRGVQLAF-IVDEggfilddfiP-NFKKPIALIAVSEKGSMNLMLQVNMTSGHSS 259
Cdd:cd03891 123 FLIT--SDEEGPAIdGTKKVLEWLKARGEKIDYcIVGE---------PtSEKKLGDTIKIGRRGSLNGKLTIKGKQGHVA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 260 APPK-ETSIGILAAAVSRLEQTPmpiiFGSGtvvtvlqqlaNEFpfpvniilsnpwlFEPlisrfmernpltnaiirTTT 338
Cdd:cd03891 192 YPHLaDNPIHLLAPILAELTATV----LDEG----------NEF-------------FPP-----------------SSL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 339 ALTIFKAGVKF-NVIPPVAQATVNFRIHPGQTVQEVLELTKNIVADNRVQFHVLSAFDPLP-VSPSDDKAlgyQLLRQTV 416
Cdd:cd03891 228 QITNIDVGNGAtNVIPGELKAKFNIRFNDEHTGESLKARIEAILDKHGLDYDLEWKLSGEPfLTKPGKLV---DAVSAAI 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 417 QSV---FPEVNitapvTSIGNTDSRFFTNLTTGIYRFYPIYiqpedfKRIHGVNEKISVQ 473
Cdd:cd03891 305 KEVtgiTPELS-----TSGGTSDARFIASYGCPVVEFGLVN------ATIHKVNERVSVA 353
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
112-488 |
1.14e-17 |
|
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a large variety of enzymes, including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase), canosinase, DUG2 type proteins, as well as many proteins inferred by homology to be dipeptidases. These enzymes have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. Substrates of CNDP are varied and not limited to Xaa-His dipeptides. DUG2 proteins contain a metallopeptidase domain and a large N-terminal WD40 repeat region, and are involved in the alternative pathway of glutathione degradation.
Pssm-ID: 349888 [Multi-domain] Cd Length: 426 Bit Score: 85.07 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 112 GSDPSLQPYLLMAHFDVVPA-PEEGWEVPPFSGLERDGIIYGRGTLDDKNSVMallqaLELLLIRKY------IPRRSFF 184
Cdd:cd03893 58 PGAPGAPTVLLYGHYDVQPAgDEDGWDSDPFELTERDGRLYGRGAADDKGPIL-----AHLAALRALmqqggdLPVNVKF 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 185 ISLGHDEESSGTGAQRISALLQSRGVQLAFIVDegGFILDDFIPNfkkpialIAVSEKGSMNLMLQVN-----MTSGHSS 259
Cdd:cd03893 133 IIEGEEESGSPSLDQLVEAHRDLLAADAIVISD--STWVGQEQPT-------LTYGLRGNANFDVEVKgldhdLHSGLYG 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 260 APPKEtSIGILAAAVSRLE----QTPMPIIFGSG-----TVVTVLQQLANEFPFPVNIIlsnpwlfEPLISRFMERNPLt 330
Cdd:cd03893 204 GVVPD-PMTALAQLLASLRdetgRILVPGLYDAVrelpeEEFRLDAGVLEEVEIIGGTT-------GSVAERLWTRPAL- 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 331 naiirTTTALTIFKAGVK-FNVIPPVAQATVNFRIHPGQTVQEVLE-----LTKNIVADNRVQFHVLSAFDPLpVSPSDD 404
Cdd:cd03893 275 -----TVLGIDGGFPGEGsKTVIPPRARAKISIRLVPGQDPEEASRlleahLEKHAPSGAKVTVSYVEGGMPW-RSDPSD 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 405 KAlgYQLLRQTVQSVFPevnITAPVTSIGNT-----DSRFFTNLTTGIYRFypiyIQPEDfkRIHGVNEKISVQAYETQV 479
Cdd:cd03893 349 PA--YQAAKDALRTAYG---VEPPLTREGGSipfisVLQEFPQAPVLLIGV----GDPDD--NAHSPNESLRLGNYKEGT 417
|
....*....
gi 269846968 480 KFIFELIQN 488
Cdd:cd03893 418 QAEAALLYS 426
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
107-453 |
1.45e-17 |
|
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; acylase I; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. Acylase I is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate) and is considered as a potential target of antimicrobial agents. Porcine AcyI is also shown to deacetylate certain quorum-sensing N-acylhomoserine lactones, while the rat enzyme has been implicated in degradation of chemotactic peptides of commensal bacteria. Prokaryotic arginine synthesis usually involves the transfer of an acetyl group to glutamate by ornithine acetyltransferase in order to form ornithine. However, Escherichia coli acetylornithine deacetylase (acetylornithinase, ArgE) (EC 3.5.1.16) catalyzes the deacylation of N2-acetyl-L-ornithine to yield ornithine and acetate. Phylogenetic evidence suggests that the clustering of the arg genes in one continuous sequence pattern arose in an ancestor common to Enterobacteriaceae and Vibrionaceae, where ornithine acetyltransferase was lost and replaced by a deacylase. Elevated levels of serum aminoacylase-1 autoantibody have been seen in the disease progression of chronic hepatitis B (CHB), making ACY1 autoantibody a valuable serum biomarker for discriminating hepatitis B virus (HBV) related liver cirrhosis from CHB.
Pssm-ID: 349898 [Multi-domain] Cd Length: 391 Bit Score: 84.63 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 107 LFTIQGSDPSLQPYLLMAHFDVVPAPEEGWEVPPFSG-LERDGIIYGRGTLDDKNSVMALLQALELLLIRKYIPRRSFFI 185
Cdd:cd05646 54 VLTWEGSNPELPSILLNSHTDVVPVFEEKWTHDPFSAhKDEDGNIYARGAQDMKCVGIQYLEAIRRLKASGFKPKRTIHL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 186 SLGHDEESSG-TGAQRISALLQSRGVQLAFIVDEGGFILDDFIPNFkkpialiaVSEKGSMNLMLQVNMTSGHSSappke 264
Cdd:cd05646 134 SFVPDEEIGGhDGMEKFVKTEEFKKLNVGFALDEGLASPTEEYRVF--------YGERSPWWVVITAPGTPGHGS----- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 265 tsigilaaavsrleqtpmpiIFGSGTVVTVLQQLANefpfpvniilsnpwlfepLISRF-------MERNP-LTNAIIrT 336
Cdd:cd05646 201 --------------------KLLENTAGEKLRKVIE------------------SIMEFresqkqrLKSNPnLTLGDV-T 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 337 TTALTIFKAGVKFNVIPPVAQATVNFRIHPGQTVQEVLELTKNIVAD--NRVQFHVLSAFDPLPVSPSDDKALGYQLLRQ 414
Cdd:cd05646 242 TVNLTMLKGGVQMNVVPSEAEAGFDLRIPPTVDLEEFEKQIDEWCAEagRGVTYEFEQKSPEKDPTSLDDSNPWWAAFKK 321
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 269846968 415 TVQsvfpEVNITA-PVTSIGNTDSRFFTNLTTGIYRFYPI 453
Cdd:cd05646 322 AVK----EMGLKLkPEIFPAATDSRYIRALGIPALGFSPM 357
|
|
| dapE_proteo |
TIGR01246 |
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a ... |
125-476 |
1.55e-15 |
|
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a proteobacterial subset of succinyl-diaminopimelate desuccinylases. An experimentally confirmed Gram-positive lineage succinyl-diaminopimelate desuccinylase has been described for Corynebacterium glutamicum (SP:Q59284), and a neighbor-joining tree shows the seed members, SP:Q59284, and putative archaeal members such as TrEMBL:O58003 in a single clade. However, the archaeal members differ substantially, share a number of motifs with acetylornithine deacetylases rather than succinyl-diaminopimelate desuccinylases, and are not taken as trusted examples of succinyl-diaminopimelate desuccinylases. This model is limited to proteobacterial members for this reason. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 162269 [Multi-domain] Cd Length: 370 Bit Score: 78.22 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 125 HFDVVPA-PEEGWEVPPFSGLERDGIIYGRGTLDDKNSV--MALLQALELLLIRKYIPRRSFFISlgHDEESSGT-GAQR 200
Cdd:TIGR01246 63 HTDVVPAgPEEQWSSPPFEPVERDGKLYGRGAADMKGSLaaFIVAAERFVKKNPDHKGSISLLIT--SDEEGTAIdGTKK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 201 ISALLQSRGVQLAF-IVDEggfilddfiPNFKKPIA-LIAVSEKGSMNLMLQVNMTSGHSSAPpketsigilaaavsRLE 278
Cdd:TIGR01246 141 VVETLMARDELIDYcIVGE---------PSSVKKLGdVIKNGRRGSITGNLTIKGIQGHVAYP--------------HLA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 279 QTPMPiifgsgTVVTVLQQLA-------NEFPFPVNIILSNpwlfeplisrfmernpltnaiIRTTTALTifkagvkfNV 351
Cdd:TIGR01246 198 NNPIH------KAAPALAELTaikwdegNEFFPPTSLQITN---------------------IHAGTGAN--------NV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 352 IPPVAQATVNFRIHPGQTVQEVLELTKNIVADNRVQFHVLSAFDPLPVSPSDDKalgyqlLRQTVQSVFPEVNITAPV-- 429
Cdd:TIGR01246 243 IPGELYVQFNLRFSTEVSDEILKQRVEAILDQHGLDYDLEWSLSGEPFLTNDGK------LIDKAREAIEETNGIKPEls 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 269846968 430 TSIGNTDSRFFTNLTTGIYRFYPIYiqpedfKRIHGVNEKISVQAYE 476
Cdd:TIGR01246 317 TGGGTSDGRFIALMGAEVVEFGPVN------ATIHKVNECVSIEDLE 357
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
53-403 |
9.09e-14 |
|
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase (ArgE, Acetylornithinase, AO, N2-acetyl-L-ornithine amidohydrolase, EC 3.5.1.16) subfamily. ArgE catalyzes the conversion of N-acetylornithine to ornithine, which can then be incorporated into the urea cycle for the final stage of arginine synthesis. The substrate specificity of ArgE is quite broad; several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved.
Pssm-ID: 349889 [Multi-domain] Cd Length: 367 Bit Score: 72.63 E-value: 9.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 53 EALKGAIQIPTVTFSSEKsnttALAEfgkYIHKVFPTV-VSTSFIQHEVVEEYSHLFTIqgsDPSLQP-YLLMAHFDVVP 130
Cdd:cd03894 1 ELLARLVAFDTVSRNSNL----ALIE---YVADYLAALgVKSRRVPVPEGGKANLLATL---GPGGEGgLLLSGHTDVVP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 131 APEEGWEVPPFSGLERDGIIYGRGTLDDKNSVMALLQALELLLIRKyiPRRSFFISLGHDEESSGTGAQRISALLQSRGV 210
Cdd:cd03894 71 VDGQKWSSDPFTLTERDGRLYGRGTCDMKGFLAAVLAAVPRLLAAK--LRKPLHLAFSYDEEVGCLGVRHLIAALAARGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 211 Q-LAFIVDEggfilddfiPNFKKPIaliaVSEKGSMNLMLQVNMTSGHSSAPPKetsigilaaAVSRLEQtpmpiifgSG 289
Cdd:cd03894 149 RpDAAIVGE---------PTSLQPV----VAHKGIASYRIRVRGRAAHSSLPPL---------GVNAIEA--------AA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 290 TVVTVLQQLANEFpfpvniilsnpwLFEPLISRFmernpltnAIIRTTTALTIFKAGVKFNVIPPVAQATVNFRIHPGQT 369
Cdd:cd03894 199 RLIGKLRELADRL------------APGLRDPPF--------DPPYPTLNVGLIHGGNAVNIVPAECEFEFEFRPLPGED 258
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 269846968 370 VQEVLELTKNIVA------DNRVQFHVLSAFDPLPVSPSD 403
Cdd:cd03894 259 PEAIDARLRDYAEallefpEAGIEVEPLFEVPGLETDEDA 298
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
87-414 |
2.08e-13 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 71.76 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 87 FPTVVSTS---FIqhEVVEEY-------SHLF------------TIQGSDPSLqpYLLMAHFDVVPAPEEGWEVPPFSGL 144
Cdd:PRK07522 16 FDTVSRDSnlaLI--EWVRDYlaahgveSELIpdpegdkanlfaTIGPADRGG--IVLSGHTDVVPVDGQAWTSDPFRLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 145 ERDGIIYGRGTLDDKN---SVMALLQALELLLIRKYIprrsfFISLGHDEESSGTGAQRISALLQSRGVQ-LAFIVDEgg 220
Cdd:PRK07522 92 ERDGRLYGRGTCDMKGfiaAALAAVPELAAAPLRRPL-----HLAFSYDEEVGCLGVPSMIARLPERGVKpAGCIVGE-- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 221 filddfiPNFKKPIaliaVSEKGSMNLMLQVNMTSGHSSAPPKetsiG---ILAAAvsRLeqtpmpiifgsgtvVTVLQQ 297
Cdd:PRK07522 165 -------PTSMRPV----VGHKGKAAYRCTVRGRAAHSSLAPQ----GvnaIEYAA--RL--------------IAHLRD 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 298 LANEF----PFpvniilsNPwLFEPlisrfmernPLTnaiirTTTALTIfKAGVKFNVIPPVAQATVNFRIHPGQTVQEV 373
Cdd:PRK07522 214 LADRLaapgPF-------DA-LFDP---------PYS-----TLQTGTI-QGGTALNIVPAECEFDFEFRNLPGDDPEAI 270
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 269846968 374 LE------------LTKNIVADNRVQFHVLSAFDPLPVSPSDDKAlgyQLLRQ 414
Cdd:PRK07522 271 LArirayaeaellpEMRAVHPEAAIEFEPLSAYPGLDTAEDAAAA---RLVRA 320
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
122-463 |
9.85e-13 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial and archaeal, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349901 [Multi-domain] Cd Length: 389 Bit Score: 69.79 E-value: 9.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 122 LMAHFDVVPAPEEG-WEVPPFSGLERDGIIYGRGTLDDKNSVMALLQALELLLIRKYIPRRSFFISLGHDEEssgTGAQR 200
Cdd:cd05650 74 IISHLDTVPPGDLSlWETDPWEPVVKDGKIYGRGVEDNQQGIVSSLLALKAIIKNGITPKYNFGLLFVADEE---DGSEY 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 201 -ISALLQSRGVqlafivdeggFILDDFI--PNFKKPI-ALIAVSEKGSMNLMLQVNMTSGHSSAPpkETSIGILAAAVSr 276
Cdd:cd05650 151 gIQYLLNKFDL----------FKKDDLIivPDFGTEDgEFIEIAEKSILWIKVNVKGKQCHASTP--ENGINAFVAASN- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 277 leqtpmpiifgsgtVVTVLQQLANEFPFPVNIILSNPW-LFEPlisrfmernpltnaiirtttalTIFKAGV-KFNVIPP 354
Cdd:cd05650 218 --------------FALELDELLHEKFDEKDDLFNPPYsTFEP----------------------TKKEANVpNVNTIPG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 355 VAQATVNFRIHPGQTVQEVLELTKNIVAD------NRVQFHVLSAFDPLPVSPSDDKALgyQLLRQTVQSVFpevNITAP 428
Cdd:cd05650 262 YDVFYFDCRVLPTYKLDEVLKFVNKIISDfensygAGITYEIVQKEQAPPATPEDSEIV--VRLSKAIKKVR---GREAK 336
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 269846968 429 VTSI-GNTDSRFFTnlttgiYRFYPIYI---------QPEDFKRI 463
Cdd:cd05650 337 LIGIgGGTVAAFLR------KKGYPAVVwstldetahQPNEYIRI 375
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
111-238 |
1.50e-12 |
|
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and signaling pathways throughout all kingdoms of life. This hierarchy contains zinc peptidases that correspond to the MH clan in the MEROPS database, which contains 4 families (M18, M20, M28, M42). The peptidase M20 family includes carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase. The dipeptidases include bacterial dipeptidase, peptidase V (PepV), a non-specific eukaryotic dipeptidase, and two Xaa-His dipeptidases (carnosinases). There is also the bacterial aminopeptidase, peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. Peptidase family M28 contains aminopeptidases and carboxypeptidases, and has co-catalytic zinc ions. However, several enzymes in this family utilize other first row transition metal ions such as cobalt and manganese. Each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The aminopeptidases in this family are also called bacterial leucyl aminopeptidases, but are able to release a variety of N-terminal amino acids. IAP aminopeptidase and aminopeptidase Y preferentially release basic amino acids while glutamate carboxypeptidase II preferentially releases C-terminal glutamates. Glutamate carboxypeptidase II and plasma glutamate carboxypeptidase hydrolyze dipeptides. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 is widely distributed in bacteria and eukaryotes. However, only yeast aminopeptidase I and mammalian aspartyl aminopeptidase have been characterized in detail. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues).
Pssm-ID: 349870 [Multi-domain] Cd Length: 200 Bit Score: 66.29 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 111 QGSDPSLQPYLLMAHFDVVPAPEEGWEVPPFSGL-ERDGIIYGRGTLDDKNSVMALLQALELLLIRKYIPRRSFFISLGH 189
Cdd:cd03873 6 LGGGEGGKSVALGAHLDVVPAGEGDNRDPPFAEDtEEEGRLYGRGALDDKGGVAAALEALKRLKENGFKPKGTIVVAFTA 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 269846968 190 DEE---SSGTGAQRISALLQSRGVQLAFIVDEGGFILDDFIPNFKKPIALIA 238
Cdd:cd03873 86 DEEvgsGGGKGLLSKFLLAEDLKVDAAFVIDATAGPILQKGVVIRNPLVDAL 137
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
107-222 |
4.34e-12 |
|
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family corresponds to the MEROPS MH clan families M18, M20, and M42. The peptidase M20 family contains exopeptidases, including carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase, dipeptidases such as bacterial dipeptidase, peptidase V (PepV), a eukaryotic, non-specific dipeptidase, and two Xaa-His dipeptidases (carnosinases). This family also includes the bacterial aminopeptidase peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. These peptidases generally hydrolyze the late products of protein degradation so as to complete the conversion of proteins to free amino acids. Glutamate carboxypeptidase hydrolyzes folate analogs such as methotrexate, and therefore can be used to treat methotrexate toxicity. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 (aspartyl aminopeptidase, DAP) family cleaves only unblocked N-terminal acidic amino-acid residues and is highly selective for hydrolyzing aspartate or glutamate residues. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues).
Pssm-ID: 349948 [Multi-domain] Cd Length: 198 Bit Score: 65.15 E-value: 4.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 107 LFTIQGSDPSLQPYLLMAHFDVVPAPEEGWEVPPFSGL-ERDGIIYGRGTLDDKNSVMALLQALELLLIRKYIPRRSFFI 185
Cdd:cd18669 2 VIARYGGGGGGKRVLLGAHIDVVPAGEGDPRDPPFFVDtVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLKGTVVV 81
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 269846968 186 SLGHDEESSGTGAQ-RISALLQSR--GVQLAFIVDEGGFI 222
Cdd:cd18669 82 AFTPDEEVGSGAGKgLLSKDALEEdlKVDYLFVGDATPAP 121
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
124-194 |
6.64e-12 |
|
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, Peptidase V (Xaa-His dipeptidase; PepV g.p. (Lactobacillus lactis); X-His dipeptidase; beta-Ala-His dipeptidase; carnosinase) subfamily. The PepV group of proteins is widely distributed in lactic acid bacteria. PepV, along with PepT, functions at the end of the proteolytic processing system. PepV is a monomeric metalloenzyme that preferentially degrades hydrophobic dipeptides. The Streptococcus gordonii PepV gene is homologous to the PepV gene family from Lactobacillus and Lactococcus spp. PepV recognizes and fixes the dipeptide backbone, while the side chains are not specifically probed and can vary, rendering it a nonspecific dipeptidase. It has been shown that Lactococcus lactis subspecies lactis (L9) PepV does not hydrolyze dipeptides containing Pro or D-amino acids at the C-terminus, while PepV from Lactobaccilus has been shown to have L-carnosine hydrolyzing activity. The mammalian PepV also acts on anserine and homocarnosine (but not on homoanserine), and to a lesser extent on some other aminoacyl-L-histidine dipeptides. Also included is the Staphylococcus aureus metallopeptidase, Sapep, a Mn(2+)-dependent dipeptidase where large interdomain movements could potentially regulate the activity of this enzyme.
Pssm-ID: 349884 [Multi-domain] Cd Length: 449 Bit Score: 67.27 E-value: 6.64e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 269846968 124 AHFDVVPApEEGWEVPPFSGLERDGIIYGRGTLDDKNSVMALLQALelllirKYI------PRRSFFISLGHDEESS 194
Cdd:cd03888 78 GHLDVVPA-GEGWTTDPFKPVIKDGKLYGRGTIDDKGPTIAALYAL------KILkdlglpLKKKIRLIFGTDEETG 147
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
121-163 |
1.13e-11 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 66.85 E-value: 1.13e-11
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 269846968 121 LLMAHFDVVPAP-EEGWEVPPFSGLERDGIIYGRGTLDDKNSVM 163
Cdd:PRK07907 87 LLYAHHDVQPPGdPDAWDSPPFELTERDGRLYGRGAADDKGGIA 130
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
112-488 |
5.80e-11 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. This family includes Sso-CP2 from Sulfolobus solfataricus.
Pssm-ID: 349930 [Multi-domain] Cd Length: 429 Bit Score: 64.28 E-value: 5.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 112 GSDPSLqpyLLMAHFDVVPA-PEEGWEVPPFSGLERDGIIYGRGTLDDKNSVMallqaLELLLIRKY------IPRRSFF 184
Cdd:cd05681 57 GDAKTL---LFYNHYDVQPAePLELWTSDPFELTIRNGKLYARGVADDKGELM-----ARLAALRALlqhlgeLPVNIKF 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 185 ISLGHDEESSGT---GAQRISALLQSRGVqlafiVDEGGFIlddfipNFK-KPIalIAVSEKGSMNLMLQVNMTSG--HS 258
Cdd:cd05681 129 LVEGEEEVGSPNlekFVAEHADLLKADGC-----IWEGGGK------NPKgRPQ--ISLGVKGIVYVELRVKTADFdlHS 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 259 S-APPKETSIGILAAAVSRLEqtpmpiifGSGTVVTV-------------LQQLANEFPFPVNIILSNPWLFEPLISRFM 324
Cdd:cd05681 196 SyGAIVENPAWRLVQALNSLR--------DEDGRVLIpgfyddvrplseaERALIDTYDFDPEELRKTYGLKRPLQVEGK 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 325 ERNpltnaiIRTTTALTI----FKAG-----VKfNVIPPVAQATVNFRIHPGQTVQEVLELTKNIVADN---RVQFHVLS 392
Cdd:cd05681 268 DPL------RALFTEPTCningIYSGytgegSK-TILPSEAFAKLDFRLVPDQDPAKILSLLRKHLDKNgfdDIEIHDLL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 393 AFDPLPVSPSDDKAlgyQLLRQTVQSVFPEVNITAPVTSIGNTDSRFFTNLTTGIYRFYPIYIQpedfKRIHGVNEKISV 472
Cdd:cd05681 341 GEKPFRTDPDAPFV---QAVIESAKEVYGQDPIVLPNSAGTGPMYPFYDALEVPVVAIGVGNAG----SNAHAPNENIRI 413
|
410
....*....|....*.
gi 269846968 473 QAYETQVKFIFELIQN 488
Cdd:cd05681 414 ADYYKGIEHTEELLRN 429
|
|
| dipeptidaselike |
TIGR01887 |
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
53-193 |
1.16e-10 |
|
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely related to the characterized non-specific dipeptidase, PepV. Many enzymes in this clade have been given names including the terms "Xaa-His" and "carnosinase" due to the early mis-characterization of the Lactobacillus delbrueckii PepV enzyme. These names are likely too specific.
Pssm-ID: 273854 [Multi-domain] Cd Length: 447 Bit Score: 63.55 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 53 EALKGAIQIPTVTFSSEKSNTtalAEFGKYIHKVFPTVVSTS----FIQHEVVEEYSHLFTIQGSDpslqpYL-LMAHFD 127
Cdd:TIGR01887 6 EDLKELIAIDSVEDLEKAKEG---APFGEGPRKALDKFLEIAkrdgFTTENVDNYAGYIEYGQGEE-----VLgILGHLD 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 269846968 128 VVPApEEGWEVPPFSGLERDGIIYGRGTLDDKNSVMALLQALELLLIRKYIPRRSFFISLGHDEES 193
Cdd:TIGR01887 78 VVPA-GDGWTSPPFEPTIKDGRIYGRGTLDDKGPTIAAYYAMKILKELGLKLKKKIRFIFGTDEES 142
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
125-472 |
2.07e-10 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 62.41 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 125 HFDVVPA-PEEGWEVPPFSGLERDGIIYGRGTLDDKNSV--MallQALELLLIRKYIPRR---SFFISlgHDEESSGT-G 197
Cdd:PRK13009 66 HTDVVPPgDLEAWTSPPFEPTIRDGMLYGRGAADMKGSLaaF---VVAAERFVAAHPDHKgsiAFLIT--SDEEGPAInG 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 198 AQRISALLQSRGVQLAF-IVDE-------GgfildDFIPNfkkpialiavSEKGSMNLMLQVNMTSGHSSAP-----Pke 264
Cdd:PRK13009 141 TVKVLEWLKARGEKIDYcIVGEptsterlG-----DVIKN----------GRRGSLTGKLTVKGVQGHVAYPhladnP-- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 265 tsIGILAAAVSRLEQTPmpiiFGSGtvvtvlqqlaNEFpfpvniilsnpwlFEPlisrfmernpltnaiirTTTALTIFK 344
Cdd:PRK13009 204 --IHLAAPALAELAATE----WDEG----------NEF-------------FPP-----------------TSLQITNID 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 345 AGVK-FNVIPPVAQATVNFRIHPGQTVQEVLELTKNIVADNRVQFHV---LSAfDPLPVSPSDdkalgyqLLRQTVQSVF 420
Cdd:PRK13009 238 AGTGaTNVIPGELEAQFNFRFSTEHTAESLKARVEAILDKHGLDYTLewtLSG-EPFLTPPGK-------LVDAVVAAIE 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 269846968 421 PEVNITA-PVTSIGNTDSRFFTNLTTGIYRFYPIYiqpedfKRIHGVNEKISV 472
Cdd:PRK13009 310 AVTGITPeLSTSGGTSDARFIADYGAQVVEFGPVN------ATIHKVNECVSV 356
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
125-486 |
2.43e-10 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 62.21 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 125 HFDVVPAP-EEGWEVPPFSGLERDGIIYGRGTLDDKNSVM---------ALLQALELLLIRkyiprrsFFISLGhdEESS 194
Cdd:PRK08588 67 HMDVVAAGdVDKWTYDPFELTEKDGKLYGRGATDMKSGLAalviamielKEQGQLLNGTIR-------LLATAG--EEVG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 195 GTGAQRisalLQSRGV--QL-AFIVDE--GGFilddfipnfkkpialIAVSEKGSMNLMLQVNMTSGHSSAPpketSIGI 269
Cdd:PRK08588 138 ELGAKQ----LTEKGYadDLdALIIGEpsGHG---------------IVYAHKGSMDYKVTSTGKAAHSSMP----ELGV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 270 laAAVSRLeqtpmpiifgsgtvVTVLQQLANEFpfpvniilsnpwlfepliSRFMERNPLTNAIIRTTtalTIFKAGVKF 349
Cdd:PRK08588 195 --NAIDPL--------------LEFYNEQKEYF------------------DSIKKHNPYLGGLTHVV---TIINGGEQV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 350 NVIPPVAQATVNFRIHPGQTVQEVLELTKNIVA------DNRVQFHVLSAFDPLPVSPSDDkalgyqlLRQTVQSVFPE- 422
Cdd:PRK08588 238 NSVPDEAELEFNIRTIPEYDNDQVISLLQEIINevnqngAAQLSLDIYSNHRPVASDKDSK-------LVQLAKDVAKSy 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 269846968 423 VNITAPVTSI-GNTDSrffTNLTTGIYRFYPIYIQPEDFKRIHGVNEKISVQAYETQVKFIFELI 486
Cdd:PRK08588 311 VGQDIPLSAIpGATDA---SSFLKKKPDFPVIIFGPGNNLTAHQVDEYVEKDMYLKFIDIYKEII 372
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
114-397 |
9.15e-10 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are bacterial, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349902 [Multi-domain] Cd Length: 341 Bit Score: 60.02 E-value: 9.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 114 DPSLQPYLLMAHFDVVPaPEEGWEVPPFSGLERDGIIYGRGTLDDKNSVMALLQALELLLiRKYIPRRSFFISLGHDEES 193
Cdd:cd05651 52 DEGKPTLLLNSHHDTVK-PNAGWTKDPFEPVEKGGKLYGLGSNDAGASVVSLLATFLHLY-SEGPLNYNLIYAASAEEEI 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 194 SGTGAqrISALLQSRG-VQLAfIVDEggfilddfiPNFKKPialiAVSEKGSMNLMLQVNMTSGHSSAPPKETSIGIlaa 272
Cdd:cd05651 130 SGKNG--IESLLPHLPpLDLA-IVGE---------PTEMQP----AIAEKGLLVLDCTARGKAGHAARNEGDNAIYK--- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 273 avsrleqtpmpiifgsgtVVTVLQQLANeFPFP-VNIILSNPwlfeplisrfmernpltnaiirtTTALTIFKAGVKFNV 351
Cdd:cd05651 191 ------------------ALDDIQWLRD-FRFDkVSPLLGPV-----------------------KMTVTQINAGTQHNV 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 269846968 352 IPPVAQATVNFRIHPGQTVQEVLE-LTKNIVADNRVQ-FHVLSAFDPL 397
Cdd:cd05651 229 VPDSCTFVVDIRTTEAYTNEEIFEiIRGNLKSEIKPRsFRLNSSAIPP 276
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
239-383 |
2.41e-09 |
|
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices which make up the dimerization surface of members of the M20 family of peptidases. This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases.
Pssm-ID: 400158 [Multi-domain] Cd Length: 107 Bit Score: 54.66 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 239 VSEKGSMNLMLQVNMTSGHSSAPPKETS-IGILAAAVSRLEQtpmpiifgsgtvvtvlqqlanefpfpvniilsnpwlfe 317
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSGAPGKGVNaIKLLARLLAELPA-------------------------------------- 42
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 269846968 318 plisrfmERNPLTNAIIRTTTALTIFKAGVKFNVIPPVAQATVNFRIHPGQTVQEVLELTKNIVAD 383
Cdd:pfam07687 43 -------EYGDIGFDFPRTTLNITGIEGGTATNVIPAEAEAKFDIRLLPGEDLEELLEEIEAILEK 101
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
124-159 |
2.41e-09 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 59.47 E-value: 2.41e-09
10 20 30
....*....|....*....|....*....|....*.
gi 269846968 124 AHFDVVPAPEeGWEVPPFSGLERDGIIYGRGTLDDK 159
Cdd:PRK07318 86 GHLDVVPAGD-GWDTDPYEPVIKDGKIYARGTSDDK 120
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
41-163 |
2.77e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 59.32 E-value: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 41 SQFSKEERVAMKEALKGAIQIPTVTfsSEKSNTTAlaeFGKYIHKVFPTVV----STSFIQHEVVEEYSHLFTI-QGSdp 115
Cdd:PRK07205 3 SYITEKVQDACVAAIKTLVSYPSVL--NEGENGTP---FGQAIQDVLEATLdlcqGLGFKTYLDPKGYYGYAEIgQGE-- 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 269846968 116 slQPYLLMAHFDVVPAPEEG-WEVPPFSGLERDGIIYGRGTLDDKNSVM 163
Cdd:PRK07205 76 --ELLAILCHLDVVPEGDLSdWQTPPFEAVEKDGCLFGRGTQDDKGPSM 122
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
112-163 |
3.16e-09 |
|
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase M20 family, CNDP (cytosolic nonspecific dipeptidase) subfamily including anserinase (Xaa-methyl-His dipeptidase, EC 3.4.13.5), 'serum' carnosinase (beta-alanyl-L-histidine dipeptidase; EC 3.4.13.20), and some uncharacterized proteins. Two genes, CN1 and CN2, coding for proteins that degrade carnosine (beta-alanyl-L-histidine) and homocarnosine (gamma-aminobutyric acid-L-histidine), two naturally occurring dipeptides with potential neuroprotective and neurotransmitter functions, have been identified. CN1 encodes for serum carnosinase and has narrow substrate specificity for Xaa-His dipeptides, where Xaa can be beta-alanine (carnosine), N-methyl beta-alanine, alanine, glycine and gamma-aminobutyric acid (homocarnosine). CN2 corresponds to the cytosolic nonspecific dipeptidase (CNDP; EC 3.4.13.18) and is not limited to Xaa-His dipeptides. CNDP requires Mn(2+) for full activity and does not hydrolyze homocarnosine. Anserinase is a dipeptidase that mainly catalyzes the hydrolysis of N-alpha-acetylhistidine.
Pssm-ID: 349925 [Multi-domain] Cd Length: 467 Bit Score: 59.15 E-value: 3.16e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 269846968 112 GSDPSLQPYLLMAHFDVVPA-PEEGWEVPPFSGLERDGIIYGRGTLDDKNSVM 163
Cdd:cd05676 80 GSDPSKKTVLIYGHLDVQPAkLEDGWDTDPFELTEKDGKLYGRGSTDDKGPVL 132
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
121-163 |
6.82e-09 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349929 [Multi-domain] Cd Length: 437 Bit Score: 58.09 E-value: 6.82e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 269846968 121 LLMAHFDVVPA-PEEGWEVPPFSGLERDGIIYGRGTLDDKNSVM 163
Cdd:cd05680 67 LVYGHYDVQPPdPLELWTSPPFEPVVRDGRLYARGASDDKGQVF 110
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
96-220 |
9.94e-09 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 57.48 E-value: 9.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 96 IQHEVVEE---YSHLFTIQGSDPSLqpyLLMAHFDVVPAPEEGWEVPPFSGLERDGIIYGRGTLDDKN---SVMALLQAL 169
Cdd:PRK08554 42 IESELIEKdgyYAVYGEIGEGKPKL---LFMAHFDVVPVNPEEWNTEPFKLTVKGDKAYGRGSADDKGnvaSVMLALKEL 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 269846968 170 ELLLIRKYIprrsfFISLGHDEESSGTGAQRISALLQSRGVQLAFIVDEGG 220
Cdd:PRK08554 119 SKEPLNGKV-----IFAFTGDEEIGGAMAMHIAEKLREEGKLPKYMINADG 164
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
121-162 |
1.17e-08 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 56.87 E-value: 1.17e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 269846968 121 LLM-AHFDVVPAP-EEGWEVPPFSGLERDGIIYGRGTLDDKNSV 162
Cdd:PRK13004 72 IAFdAHIDTVGIGdIKNWDFDPFEGEEDDGRIYGRGTSDQKGGM 115
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
122-440 |
4.63e-08 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 55.24 E-value: 4.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 122 LMAHFDVVPAPEEG-WEVPPFSGLERDGIIYGRGTLDDKNSVMALLQALELLLIRKYIPRRSFFISLGHDEEssgTGaqr 200
Cdd:PRK13983 81 IISHMDVVPPGDLSlWETDPFKPVVKDGKIYGRGSEDNGQGIVSSLLALKALMDLGIRPKYNLGLAFVSDEE---TG--- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 201 isallqSR-GvqLAFIVDE--GGFILDDFI--PNFKKPI-ALIAVSEKGSMNLMLQVNMTSGHSSAPPKetsiGILAAAV 274
Cdd:PRK13983 155 ------SKyG--IQYLLKKhpELFKKDDLIlvPDAGNPDgSFIEIAEKSILWLKFTVKGKQCHASTPEN----GINAHRA 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 275 srleqtpmpiifgsgtvvtvlqqlANEFpfpvniILSnpwLFEPLISRFMERNPLTNAIIrTTTALTIFKAGVK-FNVIP 353
Cdd:PRK13983 223 ------------------------AADF------ALE---LDEALHEKFNAKDPLFDPPY-STFEPTKKEANVDnINTIP 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 354 pvAQATVNF--RIHPGQTVQEVLELTKNIVAD------NRVQFHVLSAFDPLPVSPSDDKALgyQLLRQTVQSVFpevNI 425
Cdd:PRK13983 269 --GRDVFYFdcRVLPDYDLDEVLKDIKEIADEfeeeygVKIEVEIVQREQAPPPTPPDSEIV--KKLKRAIKEVR---GI 341
|
330
....*....|....*.
gi 269846968 426 TAPVTSI-GNTDSRFF 440
Cdd:PRK13983 342 EPKVGGIgGGTVAAFL 357
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
124-263 |
4.67e-08 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial and archaeal, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349900 [Multi-domain] Cd Length: 381 Bit Score: 55.12 E-value: 4.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 124 AHFDVVPAPEE-GWEVPPFSGLERDGIIYGRGTLDDKNSVMALLQALELLLIRKYIPRRSFFISLG--HDEESSGTGAQR 200
Cdd:cd05649 59 GHIDTVGIGNIdNWKFDPYEGYETDGKIYGRGTSDQKGGLASMVYAAKIMKDLGLRDFAYTILVAGtvQEEDCDGVCWQY 138
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 269846968 201 ISallQSRGVQLAFIV----DEGGfilddfipnfkkpialIAVSEKGSMNLMLQVNMTSGHSSAPPK 263
Cdd:cd05649 139 IS---KADKIKPDFVVsgepTDGN----------------IYRGQRGRMEIRVDTKGVSCHGSAPER 186
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
122-474 |
8.66e-08 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349890 [Multi-domain] Cd Length: 400 Bit Score: 54.24 E-value: 8.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 122 LMAHFDVVPA-PEEGWEVPPFSGLERDGIIYGRGTLDDKNSVMALLQALELLLIRKYIPR-RSFFISLgHDEESSGTGAq 199
Cdd:cd03895 79 LNGHIDVVPEgPVELWTRPPFEATIVDGWMYGRGAGDMKAGLAANLFALDALRAAGLQPAaDVHFQSV-VEEECTGNGA- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 200 rISALLQSRGVQLAFIVDEGGFILddfipnfkkpialiAVSEKGSMNLMLQVNMTSGHSSappkETSIGILAaavsrleq 279
Cdd:cd03895 157 -LAALMRGYRADAALIPEPTELKL--------------VRAQVGVIWFRVKVRGTPAHVA----EASEGVNA-------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 280 tpmpiIFGSGTVVTVLQQLANEfpfpvniilsnpWLFEPLISRFMERNPLTNAIirtttALTIFKAGVKFNVIPpvAQAT 359
Cdd:cd03895 210 -----IEKAMHLIQALQELERE------------WNARKKSHPHFSDHPHPINF-----NIGKIEGGDWPSSVP--AWCV 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 360 VNFRIH--PGQTVQEVLELTKNIVADNRVQFHVLSAfDPLPVSPSDDKALGYQL-----LRQTVQSVFPEVNITAPVTSI 432
Cdd:cd03895 266 LDCRIGiyPGESPEEARREIEECVADAAATDPWLSN-HPPEVEWNGFQAEGYVLepgsdAEQVLAAAHQAVFGTPPVQSA 344
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 269846968 433 --GNTDSRFFtnlttGIYRFYP-IYIQPEDfKRIHGVNEKISVQA 474
Cdd:cd03895 345 mtATTDGRFF-----VLYGDIPaLCYGPGS-RDAHGFDESVDLES 383
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
45-162 |
1.98e-07 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 53.21 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 45 KEERVAMKEALKGAIQIPTVTFSSE-KSNTTALAEF--GKYIHKVFPTVVSTSFIQHEVV-EEYSHlftiqgsDPSLQPY 120
Cdd:PRK08201 10 RERREAHLEELKEFLRIPSISALSEhKEDVRKAAEWlaGALEKAGLEHVEIMETAGHPIVyADWLH-------APGKPTV 82
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 269846968 121 LLMAHFDVVPA-PEEGWEVPPFSGLERDGIIYGRGTLDDKNSV 162
Cdd:PRK08201 83 LIYGHYDVQPVdPLNLWETPPFEPTIRDGKLYARGASDDKGQV 125
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
52-480 |
1.43e-06 |
|
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, acetylornithine deacetylase (ArgE)/acetyl-lysine deacetylase (LysK) subfamily. Proteins in this subfamily are mainly archaeal with related bacterial species and are deacetylases with specificity for both N-acetyl-ornithine and N-acetyl-lysine found within a lysine biosynthesis operon. ArgE catalyzes the conversion of N-acetylornithine to ornithine, while LysK, a homolog of ArgE, has deacetylating activities for both N-acetyllysine and N-acetylornithine at almost equal efficiency. These results suggest that LysK which may share an ancestor with ArgE functions not only for lysine biosynthesis, but also for arginine biosynthesis in species such as Thermus thermophilus. The substrate specificity of ArgE is quite broad in that several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved.
Pssm-ID: 349904 [Multi-domain] Cd Length: 343 Bit Score: 50.43 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 52 KEALKGAIQIPTVTFSSEKSNTTALAEFGKYIHKVFptvvstsfiqhevVEEYSHLFTIQGSDPSLqpYLLMAHFDVVPA 131
Cdd:cd05653 4 VELLLDLLSIYSPSGEEARAAKFLEEIMKELGLEAW-------------VDEAGNAVGGAGSGPPD--VLLLGHIDTVPG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 132 peegwEVPPfsgLERDGIIYGRGTLDDKNSVMALLQALELLLIRKYIprRSFFISLGhDEESSGTGAQrisALLQSRGVQ 211
Cdd:cd05653 69 -----EIPV---RVEGGVLYGRGAVDAKGPLAAMILAASALNEELGA--RVVVAGLV-DEEGSSKGAR---ELVRRGPRP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 212 LAFIVDEggfilddfipnfkkPIAL--IAVSEKGSMNLMLQVNMTSGHSSApPKETSIGILAAAVSRLEQTPMPIIFGSG 289
Cdd:cd05653 135 DYIIIGE--------------PSGWdgITLGYRGSLLVKIRCEGRSGHSSS-PERNAAEDLIKKWLEVKKWAEGYNVGGR 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 290 TVVTVLqqlanefpfpvniilsnpwlfeplisrfmernpltnaiirtttaLTIFKAGVKFNVIPPVAQATVNFRIHPGQT 369
Cdd:cd05653 200 DFDSVV--------------------------------------------PTLIKGGESSNGLPQRAEATIDLRLPPRLS 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 370 VQEVLELtknivADNRVQFHVLSAFD---PLPVSPSDD--KALGYQLLRQTVQSVF------PEVNITAPvtsigntdsr 438
Cdd:cd05653 236 PEEAIAL-----ATALLPTCELEFIDdtePVKVSKNNPlaRAFRRAIRKQGGKPRLkrktgtSDMNVLAP---------- 300
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 269846968 439 fftNLTTGIYRFypiyiQPEDFKRIHGVNEKISVQAYETQVK 480
Cdd:cd05653 301 ---LWTVPIVAY-----GPGDSTLDHTPNEHIELAEIERAAA 334
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
124-197 |
2.63e-06 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 49.76 E-value: 2.63e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 269846968 124 AHFDVVPApEEGWEVPPFSGLERDGIIYGRGTLDDKNSvMALLQALELLLIRKYIPRR-SFFISLGHDEESSGTG 197
Cdd:PRK13013 91 SHHDVVEV-GHGWTRDPFGGEVKDGRIYGRGACDMKGG-LAASIIAAEAFLAVYPDFAgSIEISGTADEESGGFG 163
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
121-159 |
2.90e-06 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 49.62 E-value: 2.90e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 269846968 121 LLMAHFDVVPA-PEEGWEVPPFSGLERDGIIYGRGTLDDK 159
Cdd:PRK06837 101 ILQGHIDVVPEgPLDLWSRPPFDPVIVDGWMYGRGAADMK 140
|
|
| PRK06915 |
PRK06915 |
peptidase; |
121-159 |
3.80e-06 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 49.30 E-value: 3.80e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 269846968 121 LLMAHFDVVPAPE-EGWEVPPFSGLERDGIIYGRGTLDDK 159
Cdd:PRK06915 97 ILNGHIDVVPEGDvNQWDHHPYSGEVIGGRIYGRGTTDMK 136
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
113-488 |
4.16e-06 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 48.99 E-value: 4.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 113 SDPSLqpyLLMAHFDVVPApeegwEVPPFsglERDGIIYGRGTLDDKNSVmaLLQALELLLIRKYIPRRSFFISLGHDEE 192
Cdd:PRK08652 54 SKAEL---FVEVHYDTVPV-----RAEFF---VDGVYVYGTGACDAKGGV--AAILLALEELGKEFEDLNVGIAFVSDEE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 193 SSGTGAQrisALLQSRGVQLAFIVDeggfilddfipnfkkPIAL-IAVSEKGSMNLMLQVNMTSGHSSAPPKetsigila 271
Cdd:PRK08652 121 EGGRGSA---LFAERYRPKMAIVLE---------------PTDLkVAIAHYGNLEAYVEVKGKPSHGACPES-------- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 272 aAVSRLEQTpmpiifgsgtvVTVLQQLANEFPFPVNiilsnpwLFEPLISrfmernpltnaiirtttaLTIFKAGVKFNV 351
Cdd:PRK08652 175 -GVNAIEKA-----------FEMLEKLKELLKALGK-------YFDPHIG------------------IQEIIGGSPEYS 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 352 IPPVAQATVNFRIHPGQTVQEVLELTKNIVADNRVQFHVLSAFDPLPVSPSDDKAlgyqllrQTVQSVFPEVNITAPVTS 431
Cdd:PRK08652 218 IPALCRLRLDARIPPEVEVEDVLDEIDPILDEYTVKYEYTEIWDGFELDEDEEIV-------QLLEKAMKEVGLEPEFTV 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 269846968 432 IGN-TDSRFFTnlttgiYRFY-PIYIQPEDFKRIHGVNEKISVQAYETQVKFI---FELIQN 488
Cdd:PRK08652 291 MRSwTDAINFR------YNGTkTVVWGPGELDLCHTKFERIDVREVEKAKEFLkalNEILLE 346
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
109-159 |
2.22e-05 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 46.57 E-value: 2.22e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 269846968 109 TIQGSDP-SLQPYLLMAHFDVVPA-PEEGWEVPPFSGLERDGIIYGRGTLDDK 159
Cdd:PRK08596 68 VKKGTESdAYKSLIINGHMDVAEVsADEAWETNPFEPTIKDGWLYGRGAADMK 120
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
112-163 |
2.32e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 46.67 E-value: 2.32e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 269846968 112 GSDPSLqpyLLMAHFDVVPA-PEEGWEVPPFSGLERDGIIYGRGTLDDKNSVM 163
Cdd:PRK06446 60 GAKKTL---LIYNHYDVQPVdPLSEWKRDPFSATIENGRIYARGASDNKGTLM 109
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
46-389 |
2.48e-05 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly fungal and bacterial, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349935 [Multi-domain] Cd Length: 379 Bit Score: 46.32 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 46 EERVAMKEALkgaIQIPTVTFSSEKSNTTALAEFGKYIhkvfptvvsTSFIQHEVVEEY---------SHLFTIQGSD-- 114
Cdd:cd08013 1 DDPVSLTQTL---VRINSSNPSLSATGGAGEAEIATYV---------AAWLAHRGIEAHriegtpgrpSVVGVVRGTGgg 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 115 PSLqpyLLMAHFDVVPApeEGWEVPPFSGLERDGIIYGRGTLDDKNSVmaLLQALELLLIRKYIPRRSFFISLGHDEESS 194
Cdd:cd08013 69 KSL---MLNGHIDTVTL--DGYDGDPLSGEIADGRVYGRGTLDMKGGL--AACMAALADAKEAGLRGDVILAAVADEEDA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 195 GTGAQRISAllqsRGVQL-AFIVDEggfilddfipnfkkPIAL-IAVSEKGSMNLMLQVNMTSGHSSAPpketSIGILAa 272
Cdd:cd08013 142 SLGTQEVLA----AGWRAdAAIVTE--------------PTNLqIIHAHKGFVWFEVDIHGRAAHGSRP----DLGVDA- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 273 avsrleqtpmpiIFGSGTVVTVLQQLANEFPF-PVNIILSNPWLFEPLIsrfmernpltnaiirtttaltifKAGVKFNV 351
Cdd:cd08013 199 ------------ILKAGYFLVALEEYQQELPErPVDPLLGRASVHASLI-----------------------KGGEEPSS 243
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 269846968 352 IPPVAQATVNFRIHPGQTVQEVLELTKNI---VADNRVQFH 389
Cdd:cd08013 244 YPARCTLTIERRTIPGETDESVLAELTAIlgeLAQTVPNFS 284
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
121-416 |
4.02e-05 |
|
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase M20 family, Defective in Utilization of Glutathione (DUG2) subfamily. DUG2-type proteins are metallopeptidases containing WD repeats at the N-terminus. DUG2 proteins are involved in the alternative pathway of glutathione (GSH) degradation. GSH, the major low-molecular-weight thiol compound in most eukaryotic cells, is normally degraded through the gamma-glutamyl cycle initiated by gamma-glutamyl transpeptidase. However, a novel pathway for the degradation of GSH has been characterized; it requires the participation of three genes identified in Saccharomyces cerevisiae as "defective in utilization of glutathione" genes including DUG1, DUG2, and DUG3. DUG1 encodes a probable di- or tri-peptidase identified as M20 metallopeptidase, DUG2 gene encodes a protein with a metallopeptidase domain and a large N-terminal WD40 repeat region, while DUG3 encodes a protein with a glutamine amidotransferase domain. Although dipeptides and tripeptides with a normal peptide bond, such as cys-gly or glu-cys-gly, can be hydrolyzed by the DUG1 protein, the presence of an unusual peptide bond, like in GSH, requires the participation of the DUG2 and DUG3 proteins as well. These three proteins form a GSH degradosomal complex.
Pssm-ID: 349926 [Multi-domain] Cd Length: 436 Bit Score: 45.80 E-value: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 121 LLMAHFDVVPAPEE-GWEVPPFSGLERDGIIYGRGTLDDKNSVMALLQALELLLIRKYIPRRSFFISLGhDEESSGTGAQ 199
Cdd:cd05677 75 LFYGHYDVIPAGETdGWDTDPFTLTCENGYLYGRGVSDNKGPLLAAIYAVAELFQEGELDNDVVFLIEG-EEESGSPGFK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 200 RISALLQSRGVQLAFIVDEGGFILDDFIPnfkkpiaLIAVSEKGSMNLMLQV-----NMTSGHSSAPPKETSIGiLAAAV 274
Cdd:cd05677 154 EVLRKNKELIGDIDWILLSNSYWLDDNIP-------CLNYGLRGVIHATIVVssdkpDLHSGVDGGVLREPTAD-LIKLL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 275 SRLeQTPMPII----FGSgTVVTVLQQLANEFPFPVNIIL-SNPWLFEPLISRFmeRNPltnaiirtttALTIFKagVKF 349
Cdd:cd05677 226 SKL-QDPDGRIliphFYD-PVKPLTEAERARFTAIAETALiHEDTTVDSLIAKW--RKP----------SLTVHT--VKV 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 350 N------VIPPVAQATVNFRIHPGQTVQEVLELTKNIVAD--------NRVQFHVLSAFDPLPVSPSDDkalGYQLLRQT 415
Cdd:cd05677 290 SgpgnttVIPKSASASVSIRLVPDQDLDVIKQDLTDYIQScfaelksqNHLDIEVLNEAEPWLGDPDNP---AYQILREA 366
|
.
gi 269846968 416 V 416
Cdd:cd05677 367 V 367
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
122-155 |
2.11e-04 |
|
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. These hypothetical proteins have been inferred by homology to be exopeptidases: carboxypeptidases, dipeptidases and a specialized aminopeptidase. In general, the peptidase hydrolyzes the late products of protein degradation in order to complete the conversion of proteins to free amino acids. Members of this subfamily may bind metal ions such as zinc.
Pssm-ID: 349869 [Multi-domain] Cd Length: 394 Bit Score: 43.70 E-value: 2.11e-04
10 20 30
....*....|....*....|....*....|....
gi 269846968 122 LMAHFDVVPaPEEGWEVPPFSGLERDGIIYGRGT 155
Cdd:cd02697 78 LNAHGDVVP-PGDGWTRDPYGAVVEDGVMYGRAA 110
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
125-157 |
2.22e-04 |
|
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, acetylornithine deacetylase (ArgE, Acetylornithinase, AO, N2-acetyl-L-ornithine amidohydrolase, EC 3.5.1.16)-related subfamily. Proteins in this subfamily have not yet been characterized, but have been predicted to have deacetylase activity. ArgE catalyzes the conversion of N-acetylornithine to ornithine, which can then be incorporated into the urea cycle for the final stage of arginine synthesis. The substrate specificity of ArgE is quite broad; several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved.
Pssm-ID: 349934 [Multi-domain] Cd Length: 423 Bit Score: 43.60 E-value: 2.22e-04
10 20 30
....*....|....*....|....*....|....
gi 269846968 125 HFDVVPAPEEGWEVPPFSgLERDG-IIYGRGTLD 157
Cdd:cd08012 86 HMDVVTANPETWEFDPFS-LSIDGdKLYGRGTTD 118
|
|
| PRK09104 |
PRK09104 |
hypothetical protein; Validated |
119-163 |
3.64e-04 |
|
hypothetical protein; Validated
Pssm-ID: 236379 [Multi-domain] Cd Length: 464 Bit Score: 42.97 E-value: 3.64e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 269846968 119 PYLLM-AHFDVVPA-PEEGWEVPPFS-GLERDG----IIYGRGTLDDKNSVM 163
Cdd:PRK09104 83 PHVLFyGHYDVQPVdPLDLWESPPFEpRIKETPdgrkVIVARGASDDKGQLM 134
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
121-472 |
5.81e-04 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 42.08 E-value: 5.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 121 LLMAHFDVVPapeeGWEVPPFSGLerdgIIYGRGTLDDKNSVMALLQALELLLIRKYiprrSFFISLGHDEESSGTGAQR 200
Cdd:PRK00466 64 LLASHVDTVP----GYIEPKIEGE----VIYGRGAVDAKGPLISMIIAAWLLNEKGI----KVMVSGLADEESTSIGAKE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 201 isalLQSRGVQ-LAFIVDEGGFILDdfipnfkkpialIAVSEKGSMNLMLQVNMTSGHSSApPKETSIGILAAAVsrLEQ 279
Cdd:PRK00466 132 ----LVSKGFNfKHIIVGEPSNGTD------------IVVEYRGSIQLDIMCEGTPEHSSS-AKSNLIVDISKKI--IEV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 280 TPMPIIFGSGTVVTvlqqlanefpfpvniilsnpwlfeplisrfmernpltnaiirtttalTIFKAGVKFNVIPPVAQAT 359
Cdd:PRK00466 193 YKQPENYDKPSIVP-----------------------------------------------TIIRAGESYNVTPAKLYLH 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 360 VNFRIHPGQTVQEVLELTKNIVadNRVQFHVLSAFDPLPVSPSDD--KALGYQLLRQTVQsvfPEVnitapVTSIGNTDS 437
Cdd:PRK00466 226 FDVRYAINNKRDDLISEIKDKF--QECGLKIVDETPPVKVSINNPvvKALMRALLKQNIK---PRL-----VRKAGTSDM 295
|
330 340 350
....*....|....*....|....*....|....*
gi 269846968 438 RFFTNLTTGIYRFypiyiQPEDFKRIHGVNEKISV 472
Cdd:PRK00466 296 NILQKITTSIATY-----GPGNSMLEHTNQEKITL 325
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
121-383 |
5.98e-04 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly fungal, and have been inferred by similarity as being related to both ArgE and DapE.
Pssm-ID: 349903 [Multi-domain] Cd Length: 340 Bit Score: 41.88 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 121 LLMAHFDVVPapeegwevP--PFSGLERDGIIYGRGTLDDKNSVMALLQALELLLIRKYIPRRSffISL----GhdEESS 194
Cdd:cd05652 62 LLTSHIDTVP--------PfiPYSISDGGDTIYGRGSVDAKGSVAAQIIAVEELLAEGEVPEGD--LGLlfvvG--EETG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 195 GTGAQRISALLQSRgvQLAFIVDEggfilddfiPNFKKpialIAVSEKGSMNLMLQVNMTSGHSSAPPKETS-IGILAAA 273
Cdd:cd05652 130 GDGMKAFNDLGLNT--WDAVIFGE---------PTELK----LASGHKGMLGFKLTAKGKAGHSGYPWLGISaIEILVEA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 274 VSRLEQTPMPI--IFGSGTvvtvlqqlanefpfpVNIILsnpwlfeplisrfmernpltnaiirtttaltiFKAGVKFNV 351
Cdd:cd05652 195 LVKLIDADLPSseLLGPTT---------------LNIGR--------------------------------ISGGVAANV 227
|
250 260 270
....*....|....*....|....*....|..
gi 269846968 352 IPPVAQATVNFRIHPGqtVQEVLELTKNIVAD 383
Cdd:cd05652 228 VPAAAEASVAIRLAAG--PPEVKDIVKEAVAG 257
|
|
| PRK06156 |
PRK06156 |
dipeptidase; |
124-162 |
3.39e-03 |
|
dipeptidase;
Pssm-ID: 235720 [Multi-domain] Cd Length: 520 Bit Score: 39.95 E-value: 3.39e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 269846968 124 AHFDVVPAPEEGWEVP-----PFSgLERDG-IIYGRGTLDDKNSV 162
Cdd:PRK06156 116 THADVVPANPELWVLDgtrldPFK-VTLVGdRLYGRGTEDDKGAI 159
|
|
| M20_dipept_like |
cd05679 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
64-159 |
6.02e-03 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349928 [Multi-domain] Cd Length: 448 Bit Score: 39.02 E-value: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 64 VTFSSEKSNTTALAEFGKYIHK-VFPTVVSTSF----IQHEVVEEYSHLFTIQGSDPSLQPYLLMAHFDVVPAPEEGWE- 137
Cdd:cd05679 14 VAVPTESQEPARKPELRAYLDQeMRPRFERLGFtvhiHDNPVAGRAPFLIAERIEDPSLPTLLIYGHGDVVPGYEGRWRd 93
|
90 100
....*....|....*....|...
gi 269846968 138 -VPPFSGLERDGIIYGRGTLDDK 159
Cdd:cd05679 94 gRDPWTVTVWGERWYGRGTADNK 116
|
|
| M20_Acy1_YhaA-like |
cd08021 |
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus ... |
255-441 |
9.17e-03 |
|
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus aureus amidohydrolase, SACOL0085; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). This family includes Staphylococcus aureus amidohydrolase, SACOL0085, which contains two manganese ions in the active site, and forms a homotetramer with variations in interdomain orientation which possibly plays a role in the regulation of catalytic activity.
Pssm-ID: 349941 [Multi-domain] Cd Length: 384 Bit Score: 38.41 E-value: 9.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 255 SGHSSAPpketsigilaaavsrlEQTPMPIIFGSgTVVTVLQQLanefpfpvniilsnpwlfeplISRfmERNPLTNAII 334
Cdd:cd08021 192 GGHGSMP----------------HETVDPIVIAA-QIVTALQTI---------------------VSR--RVDPLDPAVV 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269846968 335 RTTTaltiFKAGVKFNVIPPVA--QATV-----NFRIHPGQTVQEVLeltKNIVADNRVQFHvLSAFDPLPVSPSDDKAl 407
Cdd:cd08021 232 TIGT----FQGGTSFNVIPDTVelKGTVrtfdeEVREQVPKRIERIV---KGICEAYGASYE-LEYQPGYPVVYNDPEV- 302
|
170 180 190
....*....|....*....|....*....|....
gi 269846968 408 gYQLLRQTVQSVFPEVNITAPVTSIGNTDSRFFT 441
Cdd:cd08021 303 -TELVKKAAKEVLIGVENVEPQLMMGGEDFSYYL 335
|
|
| |
